| Literature DB >> 12119379 |
Jorge Nieto-Sotelo1, Luz María Martínez, Georgina Ponce, Gladys I Cassab, Alejandro Alagón, Robert B Meeley, Jean-Marcel Ribaut, Runying Yang.
Abstract
HSP101 belongs to the ClpB protein subfamily whose members promote the renaturation of protein aggregates and are essential for the induction of thermotolerance. We found that maize HSP101 accumulated in mature kernels in the absence of heat stress. At optimal temperatures, HSP101 disappeared within the first 3 days after imbibition, although its levels increased in response to heat shock. In embryonic cells, HSP101 concentrated in the nucleus and in some nucleoli. Hsp101 maps near the umc132 and npi280 markers on chromosome 6. Five maize hsp101-m-::Mu1 alleles were isolated. Mutants were null for HSP101 and defective in both induced and basal thermotolerance. Moreover, during the first 3 days after imbibition, primary roots grew faster in the mutants at optimal temperature. Thus, HSP101 is a nucleus-localized protein that, in addition to its role in thermotolerance, negatively influences the growth rate of the primary root. HSP101 is dispensable for proper embryo and whole plant development in the absence of heat stress.Entities:
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Year: 2002 PMID: 12119379 PMCID: PMC150711 DOI: 10.1105/tpc.010487
Source DB: PubMed Journal: Plant Cell ISSN: 1040-4651 Impact factor: 11.277